Effect of the intercalated cation-exchanged on the properties of nanocomposites prepared by 2-aminobenzene sulfonic acid with aniline and montmorillonite

Polymer/montmorillonite nanocomposites were prepared. Intercalation of 2-aminobenzene sulfonic acid with aniline monomers into montmorillonite modified by cation was followed by subsequent oxidative polymerization of monomers in the interlayer spacing. The clay was prepared by cation exchange process between sodium cation in (M–Na) and copper cation (M–Cu). XRD analyses show the manifestation of a basal spacing (d-spacing) for M–Cu changes depending on the inorganic cation and the polymer intercalated in the M–Cu structure. TGA analyses reveal that polymer/M–Cu composites is less stable than M–Cu. The conductivity of the composites is found to be 103 times higher than that for M–Cu. The microscopic examinations including TEM picture of the nanocomposite demonstrated an entirely different and more compatible morphology. Remarkable differences in the properties of the polymers have also been observed by UV–Vis and FTIR, suggesting that the polymer produced with presence of aniline has a higher degree of branching. The electrochemical behavior of the polymers extracted from the nanocomposites has been studied by cyclic voltammetry which indicates the electroactive effect of nanocomposite gradually increased with aniline in the polymer chain.

Expression and cellular localization of the voltage-gated calcium channel α2δ3 in the rodent retina

High-voltage-activated calcium channels are hetero-oligomeric protein complexes that mediate multiple cellular processes, including the influx of extracellular Ca2+, neurotransmitter release, gene transcription, and synaptic plasticity. These channels consist of a primary α1 pore-forming subunit, which is associated with an extracellular α2δ subunit and an intracellular β auxiliary subunit, which alter the gating properties and trafficking of the calcium channel. The cellular localization of the α2δ3 subunit in the mouse and rat retina is unknown. In this study using RT-PCR, a single band at ∼305 bp corresponding to the predicted size of the α2δ3 subunit fragment was found in mouse and rat retina and brain homogenates. Western blotting of rodent retina and brain homogenates showed a single 123-kDa band. Immunohistochemistry with an affinity-purified antibody to the α2δ3 subunit revealed immunoreactive cell bodies in the ganglion cell layer and inner nuclear layer and immunoreactive processes in the inner plexiform layer and the outer plexiform layer. α2δ3 immunoreactivity was localized to multiple cell types, including ganglion, amacrine, and bipolar cells and photoreceptors, but not horizontal cells. The expression of the α2δ3 calcium channel subunit to multiple cell types suggests that this subunit participates widely in Ca-channel-mediated signaling in the retina.